The interaction of proteins with silicic acid

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Abstract
The behavior of methemoglobin, heptadecylamine, myristic acid, stearic acid and octadecan-1-ol monolayers spread on buffers with and without silicic acid were compared. The interactions with silicic acid of bovine serum albumin, methemoglobin and poly-L-lysine were studied turbidi-metrically. The proteins and polylysine bind silicic acid most strongly at their respective isoelectric points. Heptadecylamine reacts with silicic acid between pH 5-9. Octadecanol perhaps reacts weakly. The carboxylic acids do not react. It is concluded that proteins combine with silicic acid mainly through their amino groups but subsidiary links, such as hydrogen bonds and the van der Waals forces, may also be involved.

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